Journal ArticleDOI
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
TLDR
In this review the different models of antimicrobial-peptide-induced pore formation and cell killing are presented and several observations suggest that translocated peptides can alter cytoplasmic membrane septum formation, inhibit cell-wall synthesis, inhibit nucleic-acid synthesis, inhibits protein synthesis or inhibit enzymatic activity.Abstract:
Antimicrobial peptides are an abundant and diverse group of molecules that are produced by many tissues and cell types in a variety of invertebrate, plant and animal species. Their amino acid composition, amphipathicity, cationic charge and size allow them to attach to and insert into membrane bilayers to form pores by 'barrel-stave', 'carpet' or 'toroidal-pore' mechanisms. Although these models are helpful for defining mechanisms of antimicrobial peptide activity, their relevance to how peptides damage and kill microorganisms still need to be clarified. Recently, there has been speculation that transmembrane pore formation is not the only mechanism of microbial killing. In fact several observations suggest that translocated peptides can alter cytoplasmic membrane septum formation, inhibit cell-wall synthesis, inhibit nucleic-acid synthesis, inhibit protein synthesis or inhibit enzymatic activity. In this review the different models of antimicrobial-peptide-induced pore formation and cell killing are presented.read more
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Journal ArticleDOI
The Role of Antimicrobial Peptides in Preventing Multidrug-Resistant Bacterial Infections and Biofilm Formation
TL;DR: This review was conducted to demonstrate the mode of action by which antimicrobial peptides combat multidrug-resistant bacteria and prevent biofilm formation and to introduce clinical uses of these compounds for chronic disease, medical devices, and oral health.
Journal ArticleDOI
Peptidoglycan recognition proteins are a new class of human bactericidal proteins.
TL;DR: The function of mammalian PGLyRP3 and PGLYRP4 is identified and it is shown that they are a new class of bactericidal and bacteriostatic proteins that have different structures, mechanism of actions, and expression patterns than antimicrobial peptides.
Journal ArticleDOI
Self-assembled proteins and peptides for regenerative medicine.
Journal ArticleDOI
Real-time attack on single Escherichia coli cells by the human antimicrobial peptide LL-37
TL;DR: These findings strongly suggest that disruption of the cytoplasmic membrane is not the growth-halting mechanism, and enable dissection of antimicrobial design criteria into two parts: translocation across the OM and the subsequent halting of growth.
Journal ArticleDOI
Antibacterial membrane attack by a pore-forming intestinal C-type lectin
Sohini Mukherjee,Hui Zheng,Mehabaw G. Derebe,Keith M. Callenberg,Carrie L. Partch,Darcy Rollins,Daniel C. Propheter,Josep Rizo,Michael Grabe,Qiu-Xing Jiang,Lora V. Hooper +10 more
TL;DR: It is shown that human RegIIIα (also known as HIP/PAP) binds membrane phospholipids and kills bacteria by forming a hexameric membrane-permeabilizing oligomeric pore, and a three-dimensional model of the Reg IIIα pore is derived by docking the RegIII α crystal structure into a cryo-electron microscopic map of the pore complex, and the model accords with experimentally determined properties of the pores.
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Journal ArticleDOI
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